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Alkane production from fatty alcohols by the combined reactions catalyzed by an alcohol dehydrogenase and an aldehyde-deformylating oxygenase
ABSTRACT PsADH, an alcohol dehydrogenase originating in Pantoea sp. was characterized and found to convert a broad variety of fatty alcohols into their corresponding aldehydes, the substrates of alkane biosynthesis. By coupling PsADH with NpAD, a cyanobacterial aldehyde-deformylating oxygenase, and...
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Published in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2023-07, Vol.87 (8), p.925-932 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Citations: | Items that this one cites |
Online Access: | Get full text |
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Summary: | ABSTRACT
PsADH, an alcohol dehydrogenase originating in Pantoea sp. was characterized and found to convert a broad variety of fatty alcohols into their corresponding aldehydes, the substrates of alkane biosynthesis. By coupling PsADH with NpAD, a cyanobacterial aldehyde-deformylating oxygenase, and by optimizing the conditions of the enzyme-catalyzed reactions, we achieved a 52% conversion of 1-tetradecanol to tridecane. We further applied this system to generate alkanes ranging from C5–17. These alkanes can be used as biofuels, suggesting that introducing a suitable alcohol dehydrogenase is an effective strategy to utilize fatty alcohols for alkane production.
Graphical Abstract
Graphical Abstract
By combining reactions catalyzed by an alcohol dehydrogenase and an aldehyde-deformylating oxygenase, we constructed an alkane biosynthesis process from fatty alcohols in Escherichia coli. |
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ISSN: | 1347-6947 1347-6947 |
DOI: | 10.1093/bbb/zbad056 |